N.M.R. studies on myelin basic protein. IV. 13C N.M.R. of the peptide encephalitogenic in the guinea pig

Author:

Margetson SA,Moore WJ

Abstract

The encephalitogenic nonapeptide Phe1-Ser2-Trp3-Gly4-Ala5-Glu6-Gly7-Gln8- Lys9 and its [D-Ala5] analogue have been studied in aqueous solution by 13C n.m.r. spectroscopy. The resonances of all the carbons have been assigned and their pH profiles measured. The expected conformational differences are indicated by only subtle differences in long-range pH titration shifts. The spin-lattice relaxation times T1 of all the protonated carbons of the [L-Ala5] nonapeptide have been measured at 25°C. Analysis of these data in terms of effective correlation times for side-chain mobilities suggests restricted motions for the side chains of Glu6 and Gln8 and the aromatic rings of Phe1 and Trp3.

Publisher

CSIRO Publishing

Subject

General Chemistry

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